NUSG_AQUAE
ID NUSG_AQUAE Reviewed; 248 AA.
AC O67757;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transcription termination/antitermination protein NusG {ECO:0000255|HAMAP-Rule:MF_00948};
GN Name=nusG {ECO:0000255|HAMAP-Rule:MF_00948}; OrderedLocusNames=aq_1931;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, AND DOMAIN.
RX PubMed=12198166; DOI=10.1093/emboj/cdf455;
RA Steiner T., Kaiser J.T., Marinkovic S., Huber R., Wahl M.C.;
RT "Crystal structures of transcription factor NusG in light of its nucleic
RT acid- and protein-binding activities.";
RL EMBO J. 21:4641-4653(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND SUBUNIT.
RX PubMed=12600194; DOI=10.1021/bi0272508;
RA Knowlton J.R., Bubunenko M., Andrykovitch M., Guo W., Routzahn K.M.,
RA Waugh D.S., Court D.L., Ji X.;
RT "A spring-loaded state of NusG in its functional cycle is suggested by X-
RT ray crystallography and supported by site-directed mutants.";
RL Biochemistry 42:2275-2281(2003).
CC -!- FUNCTION: Participates in transcription elongation, termination and
CC antitermination. {ECO:0000255|HAMAP-Rule:MF_00948}.
CC -!- SUBUNIT: Monomer (PubMed:12198166). Homodimer (PubMed:12600194).
CC {ECO:0000269|PubMed:12198166, ECO:0000269|PubMed:12600194}.
CC -!- DOMAIN: Contains an N-terminal RNP-like domain, a C-terminal element
CC with a KOW sequence motif and a species-specific immunoglobulin-like
CC fold. {ECO:0000269|PubMed:12198166}.
CC -!- SIMILARITY: Belongs to the NusG family. {ECO:0000255|HAMAP-
CC Rule:MF_00948}.
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DR EMBL; AE000657; AAC07722.1; -; Genomic_DNA.
DR PIR; A70466; A70466.
DR RefSeq; NP_214326.1; NC_000918.1.
DR RefSeq; WP_010881262.1; NC_000918.1.
DR PDB; 1M1G; X-ray; 2.00 A; A/B/C/D=1-248.
DR PDB; 1M1H; X-ray; 1.95 A; A=1-248.
DR PDB; 1NPP; X-ray; 2.00 A; A/B/C/D=1-248.
DR PDB; 1NPR; X-ray; 2.21 A; A=1-248.
DR PDBsum; 1M1G; -.
DR PDBsum; 1M1H; -.
DR PDBsum; 1NPP; -.
DR PDBsum; 1NPR; -.
DR AlphaFoldDB; O67757; -.
DR SMR; O67757; -.
DR STRING; 224324.aq_1931; -.
DR EnsemblBacteria; AAC07722; AAC07722; aq_1931.
DR KEGG; aae:aq_1931; -.
DR PATRIC; fig|224324.8.peg.1496; -.
DR eggNOG; COG0250; Bacteria.
DR HOGENOM; CLU_067287_1_0_0; -.
DR InParanoid; O67757; -.
DR OMA; IEGPFMN; -.
DR OrthoDB; 2027986at2; -.
DR EvolutionaryTrace; O67757; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.60.320.10; -; 1.
DR Gene3D; 3.30.70.940; -; 1.
DR HAMAP; MF_00948; NusG; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR043425; NusG-like.
DR InterPro; IPR038690; NusG_2_sf.
DR InterPro; IPR024045; NusG_dom2.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR001062; Transcrpt_antiterm_NusG.
DR InterPro; IPR015869; Transcrpt_antiterm_NusG_bac_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR30265; PTHR30265; 1.
DR PANTHER; PTHR30265:SF2; PTHR30265:SF2; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF02357; NusG; 1.
DR Pfam; PF07009; NusG_II; 1.
DR PRINTS; PR00338; NUSGTNSCPFCT.
DR SMART; SM00739; KOW; 1.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF82679; SSF82679; 1.
DR TIGRFAMs; TIGR00922; nusG; 1.
DR PROSITE; PS01014; NUSG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transcription;
KW Transcription antitermination; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..248
FT /note="Transcription termination/antitermination protein
FT NusG"
FT /id="PRO_0000113914"
FT DOMAIN 197..227
FT /note="KOW"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00948"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1M1H"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:1M1H"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1M1H"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:1M1H"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1M1H"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1NPR"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1M1H"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1M1G"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:1M1G"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1M1G"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:1M1G"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:1M1G"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:1M1G"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:1M1G"
SQ SEQUENCE 248 AA; 27999 MW; CECE083CA19D8482 CRC64;
MSEQQVQELE KKWYALQVEP GKENEAKENL LKVLELEGLK DLVDEVIVPA EEKVVIRAQG
KEKYRLSLKG NARDISVLGK KGVTTFRIEN GEVKVVESVE GDTCVNAPPI SKPGQKITCK
ENKTEAKIVL DNKIFPGYIL IKAHMNDKLL MAIEKTPHVF RPVMVGGKPV PLKEEEVQNI
LNQIKRGVKP SKVEFEKGDQ VRVIEGPFMN FTGTVEEVHP EKRKLTVMIS IFGRMTPVEL
DFDQVEKI